Proteolytic Activity at Quantum Dot-Conjugates: Kinetic Analysis Reveals Enhanced Enzyme Activity and Localized Interfacial "Hopping"

被引：115

作者：

Algar, W. Russ ^{[1
,3
]}

Malonoski, Anthony ^{[1
]}

Deschamps, Jeffrey R. ^{[1
]}

Banco-Canosa, Juan B. ^{[4
,5
]}

Susumu, Kimihiro ^{[2
]}

Stewart, Michael H. ^{[2
]}

Johnson, Brandy J. ^{[1
]}

Dawson, Philip E. ^{[4
,5
]}

Medintz, Igor L. ^{[1
]}

机构：

[1] USN, Ctr Bio Mol Sci & Engn, Res Lab, Washington, DC 20375 USA

[2] USN, Div Opt Sci, Res Lab, Washington, DC 20375 USA

[3] George Mason Univ, Coll Sci, Fairfax, VA 22030 USA

[4] Scripps Res Inst, Dept Cell Biol, La Jolla, CA 92037 USA

[5] Scripps Res Inst, Dept Chem, La Jolla, CA 92037 USA

来源：

NANO LETTERS | 2012年 / 12卷 / 07期

基金：

加拿大自然科学与工程研究理事会;

关键词：

Quantum dot; nanoparticle; peptide; proteolysis; kinetics; FRET; RESONANCE ENERGY-TRANSFER; BIOCOMPATIBLE SEMICONDUCTOR; QUANTITATIVE-ANALYSIS; GOLD NANOPARTICLES; STABILITY; LIGANDS; CHYMOTRYPSIN; PARAMETERS; INHIBITORS; CATALYSIS;

D O I：

10.1021/nl301727k

中图分类号：

O6 [化学];

学科分类号：

0703 ;

摘要：

Recent studies show that polyvalent, ligand-modified nanoparticles provide significantly enhanced binding characteristics compared to isolated ligands. Here, we assess the ability of substrate-modified nanoparticles to provide enhanced enzymatic activity. Energy transfer assays allowed quantitative, real-time measurement of proteolytic digestion at polyvalent quantum dot-peptide conjugates. Enzymatic progress curves were analyzed using an integrated Michaelis Menten (MM) formalism, revealing mechanistic details, including deviations from classic MM-behavior. A "hopping" mode of proteolysis at the nanoparticle was identified, confirming enhanced activity.

引用

页码：3793 / 3802

页数：10

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